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<h1>Humicola insolens cutinase with N-terminal His-Tag</h1>
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The Humicola insolens Cutinase (HIC) (EC 3.1.1.74, cutinase) belongs to the serine-α -β-hydrolase family (Nielsen et al., 2005) and can be used to degrade polymers like polyethylene terephthalate (Espino-Rammer et al., 2013). The catalytic pocket consists of the triad of a serine, histidine and aspartic acid (Kold et al., 2014) and the enzyme has its optimal activity at 70°C (Hunsen et al., 2008).  
 
The Humicola insolens Cutinase (HIC) (EC 3.1.1.74, cutinase) belongs to the serine-α -β-hydrolase family (Nielsen et al., 2005) and can be used to degrade polymers like polyethylene terephthalate (Espino-Rammer et al., 2013). The catalytic pocket consists of the triad of a serine, histidine and aspartic acid (Kold et al., 2014) and the enzyme has its optimal activity at 70°C (Hunsen et al., 2008).  

Revision as of 01:53, 19 September 2015

Humicola insolens cutinase with N-terminal His-Tag

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The Humicola insolens Cutinase (HIC) (EC 3.1.1.74, cutinase) belongs to the serine-α -β-hydrolase family (Nielsen et al., 2005) and can be used to degrade polymers like polyethylene terephthalate (Espino-Rammer et al., 2013). The catalytic pocket consists of the triad of a serine, histidine and aspartic acid (Kold et al., 2014) and the enzyme has its optimal activity at 70°C (Hunsen et al., 2008).

Characteristics


Molecular Weight 21068.85
Residues 200
Charge 5.5
Isoelectric Point 8.1624
A280 Molar Extinction Coefficients 12950 (reduced) 13200 (cystine bridges)
Improbability of expression in inclusion bodies 0.891
[Data taken from PEPSTATS]

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]